Structure of PDB 1gpm Chain D

Receptor sequence

>1gpmD (length=499) Species: 83333 (Escherichia coli K-12)

ENIHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPS
GIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEA
SNEREFGYAQVEVVNDSALVRGIEDALTADGKPLLDVWMSHGDKVTAIPS
DFITVASTESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDIC
QCEALWTPAKIIDDAVARIREQVGDDKVILGLSGGVDSSVTAMLLHRAIG
KNLTCVFVDNGLLRLNEAEQVLDMFGDHFGLNIVHVPAEDRFLSALAGEN
DPEAKRKIIGRVFVEVFDEEALKLEDVKWLAQGTIYPDVIEMKMGLVEPL
KELFKDEVRKIGLELGLPYDMLYRHPFPGPGLGVRVLGEVKKEYCDLLRR
ADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVE
TIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE

3D structure

• PDB: 1gpm The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
• Chain: D
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G59 C86 Y87 H181 E183 D239 K381
• Catalytic site (residue number reindexed from 1): G57 C84 Y85 H179 E181 D237 K355
• Enzyme Commision number: 6.3.5.2: GMP synthase (glutamine-hydrolyzing).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	POP	D	S235 G237 V238 D239 S240 K381	S233 G235 V236 D237 S238 K355
BS02	AMP	D	G233 L234 S235 V260 F315	G231 L232 S233 V258 F313

Gene Ontology

Molecular Function

• GO:0003921 GMP synthase activity
• GO:0003922 GMP synthase (glutamine-hydrolyzing) activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006177 GMP biosynthetic process
• GO:0006541 glutamine metabolic process
• GO:0046037 GMP metabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1gpm, PDBe:1gpm, PDBj:1gpm
• PDBsum: 1gpm
• PubMed: 8548458
• UniProt: P04079|GUAA_ECOLI GMP synthase [glutamine-hydrolyzing] (Gene Name=guaA)